Talk:Enzyme/Archive 8
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Footer
The article has sections:
- See also
- Further reading
- References
- External links
This seems quite a weighty footer, especially considering that there are also two infoboxes at the very bottom. Perhaps they could be compressed or combined? For example further reading and external links?T. Shafee (Evo&Evo) (talk) 10:20, 14 January 2014 (UTC)
Information that is in wrong section
In the 'mechanisms' section under 'Structure and Mechanisms', there's some bullet points that describe how enzymes work. The last two bullet points just say how proteins (including enzymes) tend to denature under high temperature and cease to function, which is not really related to the rest of the bullet points at all. It's correct information and I'm not trying to disagree with it, but it has nothing to do with the other bullet points or actually the 'Structure and Mechanisms' section as a whole. I don't know how to fix this stuff; can someone please take out those bullet points and put it somewhere where it makes sense?
Here's a copy/paste of the section I'm talking about
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Enzymes can act in several ways, all of which lower ΔG‡ (Gibbs energy):[39] •Lowering the activation energy by creating an environment in which the transition state is stabilized (e.g. straining the shape of a substrate—by binding the transition-state conformation of the substrate/product molecules, the enzyme distorts the bound substrate(s) into their transition state form, thereby reducing the amount of energy required to complete the transition). •Lowering the energy of the transition state, but without distorting the substrate, by creating an environment with the opposite charge distribution to that of the transition state. •Providing an alternative pathway. For example, temporarily reacting with the substrate to form an intermediate ES complex, which would be impossible in the absence of the enzyme. •Reducing the reaction entropy change by bringing substrates together in the correct orientation to react. Considering ΔH‡ alone overlooks this effect. •Increases in temperatures speed up reactions. Thus, temperature increases help the enzyme function and develop the end product even faster. However, if heated too much, the enzyme's shape deteriorates and the enzyme becomes denatured. Some enzymes like thermolabile enzymes work best at low temperatures. •The function of a protein is dependent on its structure so that if the structure is disrupted, so is its function. It is interesting that this entropic effect involves destabilization of the ground state,[40] and its contribution to catalysis is relatively small.[41] |
— Preceding unsigned comment added by 68.98.234.237 (talk) 04:00, 22 June 2014 (UTC)
Semi-protected edit request on 31 July 2014
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Add closing parenthesis after "substrates" in the first line of second paragraph:
"Enzymes act by converting starting molecules (substrates into different molecules (products)."
Michael Knudsen (talk) 07:13, 31 July 2014 (UTC)
Done Thanks for pointing that out - Arjayay (talk) 17:06, 31 July 2014 (UTC)
Is the Ribosome really the catalyst
The article states: "A small number of RNA-based biological catalysts exist, with the most common being the ribosome; these are referred to as either RNA-enzymes or ribozymes.".
Is it accurate to state that the ribosome is the catalyst? From reading the article I got the impression the ribozymes were the catalysts, and that they are smaller units within the ribosome. — Preceding unsigned comment added by 82.33.104.72 (talk) 01:24, 27 December 2014 (UTC)